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P13847 (HBSAG_HHBV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Large envelope protein
Alternative name(s):
L glycoprotein
L-HBsAg
Short name=LHB
Large S protein
Large surface protein
Major surface antigen

Cleaved into the following chain:

  1. Truncated S protein
    Short name=St
Gene names
Name:S
OrganismHeron hepatitis B virus (HHBV) [Complete proteome]
Taxonomic identifier28300 [NCBI]
Taxonomic lineageViruses › Retro-transcribing viruses › Hepadnaviridae › Avihepadnavirus
Virus hostArdeidae (herons) [TaxID: 8899]

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. The large envelope protein probably also assumes fusion between virion and host membranes. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein By similarity.

Truncated S protein may be involved in translocation of pre-S domain through the virion membrane By similarity.

Subunit structure

Large internal envelope protein interacts with capsid protein By similarity.

Subcellular location

Virion membrane.

Domain

The large envelope protein is synthesized with the pre-S region at the cytosolic side of the endoplasmic reticulum and, hence will be within the virion after budding. Therefore the pre-S region is not N-glycosylated. Later a post-translational translocation of N-terminal pre-S and TM1 domains occur in about 50% of proteins at the virion surface. These molecules change their topology by an unknown mechanism, resulting in exposure of pre-S region at virion surface.

Post-translational modification

Myristoylation contributes importantly to DHBV infectivity. It is most likely required for an early step of the life cycle involving the entry or uncoating of virus particles.

Phosphorylated on pre-S domain for about 50% of L proteins, the L chains with internal pre-S region (Li-HBsAg).

Sequence similarities

Belongs to the avihepadnavirus major surface antigen family.

Sequence caution

The sequence AAA45740.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform L (identifier: P13847-1)

Also known as: Large envelope protein; LHB; L-HBsAg;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform S (identifier: P13847-2)

Also known as: Small envelope protein; SHB; S-HBsAg;

The sequence of this isoform differs from the canonical sequence as follows:
     1-166: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 335334Large envelope protein
PRO_0000038085
Chain167 – ?24377Truncated S protein
PRO_0000322200

Regions

Topological domain2 – 241240Cytoplasmic; in intracellular conformation Potential
Topological domain2 – 167166Extracellular; in extracellular conformation Potential
Transmembrane168 – 18821Helical; Name=TM1; Note=In extracellular conformation; Potential
Topological domain189 – 24153Cytoplasmic; in extracellular conformation Potential
Transmembrane242 – 26221Helical; Name=TM2; Potential
Topological domain263 – 29533Extracellular Potential
Transmembrane296 – 31621Helical; Name=TM3; Potential
Topological domain317 – 33519Cytoplasmic Potential
Region2 – 166165Pre-S By similarity

Sites

Site?243 – ?2442Cleavage; by host Potential

Amino acid modifications

Lipidation21N-myristoyl glycine; by host By similarity
Glycosylation2651N-linked (GlcNAc...); by host Potential

Natural variations

Alternative sequence1 – 166166Missing in isoform S.
VSP_031891

Sequences

Sequence LengthMass (Da)Tools
Isoform L (Large envelope protein) (LHB) (L-HBsAg) [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: E90F7DA6A0623354

FASTA33537,219
        10         20         30         40         50         60 
MGHTQAKSTT DRRVEGGELL LQHLAGRMIP PEFSGPITTA GKFPTIQHVM DHIDSVEELR 

        70         80         90        100        110        120 
TLQAGGHWPE GTARRLGLDQ PRPTPPPITW TEEEDKKAKE FFKQYQENRP KPAETAPPPI 

       130        140        150        160        170        180 
TELHAAEPPQ WKISPEDPLL KAKALIPVKE PEVPILKVPK LTNKKKMGAT FGGILAGLIG 

       190        200        210        220        230        240 
LLVGFFLLTK ILEILRKLDW WWISLSSPKE KMLCAFQNTG AQTSPHYVGS CPWGCPGFLW 

       250        260        270        280        290        300 
TYLRLFIIFL LLLLVAAGLL FLTENKSTIF EKLQWESVSA LSSSIYSLLP SEPKSLVALT 

       310        320        330 
FGLFLIWTTS SSVTQVLVTL TQLATLSALF FKNSG

« Hide

Isoform S (Small envelope protein) (SHB) (S-HBsAg) [UniParc].

Checksum: 0FA1CFC2FAF64CD6
Show »

FASTA16918,634

References

[1]"Isolation and characterization of a hepatitis B virus endemic in herons."
Sprengel R., Kaleta E.F., Will H.
J. Virol. 62:3832-3839(1988) [PubMed: 3418788] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M22056 Genomic DNA. Translation: AAA45739.1.
M22056 Genomic DNA. Translation: AAA45740.1. Different initiation.
PIRSAVLHH. B30082.
RefSeqNP_040999.1. NC_001486.1.
NP_041000.1. NC_001486.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703546.
2703548.

Family and domain databases

InterProIPR000349. Hepvir_surfAg.
[Graphical view]
PfamPF00695. vMSA. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHBSAG_HHBV
AccessionPrimary (citable) accession number: P13847
Secondary accession number(s): Q67853
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 31, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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